Full text data of RABL6
RABL6
(C9orf86, PARF)
[Confidence: low (only semi-automatic identification from reviews)]
Rab-like protein 6 (GTP-binding protein Parf; Partner of ARF; Rab-like protein 1; RBEL1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Rab-like protein 6 (GTP-binding protein Parf; Partner of ARF; Rab-like protein 1; RBEL1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q3YEC7
ID RABL6_HUMAN Reviewed; 729 AA.
AC Q3YEC7; A8QVZ7; A8QVZ8; C6K8I4; C6K8I5; Q4F968; Q5T5R7; Q8IWK1;
read moreAC Q8TCL4; Q8WU94; Q96SR8; Q9BU21; Q9H935;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 22-JAN-2014, entry version 92.
DE RecName: Full=Rab-like protein 6;
DE AltName: Full=GTP-binding protein Parf;
DE AltName: Full=Partner of ARF;
DE AltName: Full=Rab-like protein 1;
DE Short=RBEL1;
GN Name=RABL6; Synonyms=C9orf86, PARF;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-382, FUNCTION,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CDKN2A.
RX PubMed=16582619;
RA Tompkins V., Hagen J., Zediak V.P., Quelle D.E.;
RT "Identification of novel ARF binding proteins by two-hybrid
RT screening.";
RL Cell Cycle 5:641-646(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), ALTERNATIVE SPLICING,
RP GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=17962191; DOI=10.1074/jbc.M704760200;
RA Montalbano J., Jin W., Sheikh M.S., Huang Y.;
RT "RBEL1 is a novel gene that encodes a nucleocytoplasmic Ras
RT superfamily GTP-binding protein and is overexpressed in breast
RT cancer.";
RL J. Biol. Chem. 282:37640-37649(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 6), AND SUBCELLULAR
RP LOCATION.
RX PubMed=19433581; DOI=10.1074/jbc.M109.009597;
RA Montalbano J., Lui K., Sheikh M.S., Huang Y.;
RT "Identification and characterization of RBEL1 subfamily of GTPases in
RT the Ras superfamily involved in cell growth regulation.";
RL J. Biol. Chem. 284:18129-18142(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-382.
RA Lin L., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA Wen S., Zhou G., Yang S.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
RP VARIANT GLN-382.
RC TISSUE=Brain, and Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-729 (ISOFORM 5),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-729 (ISOFORM 1), AND
RP VARIANT GLN-382.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 251-719.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-577; SER-596 AND
RP THR-599, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425 AND SER-427, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-427; SER-596
RP AND THR-599, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-427; SER-596
RP AND THR-599, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May enhance cellular proliferation. May reduce growth
CC inhibitory activity of CDKN2A.
CC -!- INTERACTION:
CC Q99750:MDFI; NbExp=2; IntAct=EBI-742029, EBI-724076;
CC P58062:SPINK7; NbExp=3; IntAct=EBI-742029, EBI-1182445;
CC -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Note=Predominantly
CC cytoplasmic.
CC -!- SUBCELLULAR LOCATION: Isoform 3: Nucleus. Note=Predominantly
CC nuclear.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=RBEL1A;
CC IsoId=Q3YEC7-1; Sequence=Displayed;
CC Note=Predominant isoform. Overexpressed in about 67% of primary
CC breast tumors;
CC Name=2;
CC IsoId=Q3YEC7-2; Sequence=VSP_022646;
CC Name=3; Synonyms=RBEL1B;
CC IsoId=Q3YEC7-3; Sequence=VSP_022649;
CC Note=No experimental confirmation available;
CC Name=4; Synonyms=RBEL1D;
CC IsoId=Q3YEC7-4; Sequence=VSP_022647, VSP_022648;
CC Name=5;
CC IsoId=Q3YEC7-5; Sequence=VSP_022646, VSP_022647, VSP_022648;
CC Name=6; Synonyms=RBEL1C;
CC IsoId=Q3YEC7-6; Sequence=VSP_042559, VSP_042560;
CC -!- PTM: Isoform 1 is O-glycosylated, while other isoforms are not.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02945.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH21095.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH35786.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14408.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB55213.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; DQ141240; AAZ73768.1; -; mRNA.
DR EMBL; EF156752; ABO84837.1; -; mRNA.
DR EMBL; EF156753; ABO84838.1; -; mRNA.
DR EMBL; GQ169126; ACS45171.1; -; mRNA.
DR EMBL; GQ169127; ACS45172.1; -; mRNA.
DR EMBL; AL355987; CAI12685.1; -; Genomic_DNA.
DR EMBL; AL355987; CAI12686.1; -; Genomic_DNA.
DR EMBL; DQ099383; AAZ13759.1; -; mRNA.
DR EMBL; BC002945; AAH02945.2; ALT_INIT; mRNA.
DR EMBL; BC021095; AAH21095.2; ALT_INIT; mRNA.
DR EMBL; BC035786; AAH35786.1; ALT_INIT; mRNA.
DR EMBL; AK023107; BAB14408.1; ALT_INIT; mRNA.
DR EMBL; AK027586; BAB55213.1; ALT_INIT; mRNA.
DR EMBL; AL713707; CAD28504.1; -; mRNA.
DR RefSeq; NP_001167459.1; NM_001173988.1.
DR RefSeq; NP_001167460.1; NM_001173989.2.
DR RefSeq; NP_078994.3; NM_024718.4.
DR UniGene; Hs.370555; -.
DR ProteinModelPortal; Q3YEC7; -.
DR SMR; Q3YEC7; 41-239.
DR IntAct; Q3YEC7; 5.
DR PhosphoSite; Q3YEC7; -.
DR DMDM; 125957950; -.
DR PaxDb; Q3YEC7; -.
DR PRIDE; Q3YEC7; -.
DR Ensembl; ENST00000311502; ENSP00000311134; ENSG00000196642.
DR Ensembl; ENST00000357466; ENSP00000350056; ENSG00000196642.
DR Ensembl; ENST00000371663; ENSP00000360727; ENSG00000196642.
DR Ensembl; ENST00000371671; ENSP00000360736; ENSG00000196642.
DR GeneID; 55684; -.
DR KEGG; hsa:55684; -.
DR UCSC; uc004cji.1; human.
DR CTD; 55684; -.
DR GeneCards; GC09P139702; -.
DR HGNC; HGNC:24703; RABL6.
DR HPA; HPA044037; -.
DR MIM; 610615; gene.
DR neXtProt; NX_Q3YEC7; -.
DR PharmGKB; PA134868176; -.
DR eggNOG; NOG138310; -.
DR HOGENOM; HOG000015428; -.
DR HOVERGEN; HBG080325; -.
DR InParanoid; Q3YEC7; -.
DR PhylomeDB; Q3YEC7; -.
DR ChiTaRS; C9orf86; human.
DR GeneWiki; C9orf86; -.
DR GenomeRNAi; 55684; -.
DR NextBio; 60481; -.
DR PRO; PR:Q3YEC7; -.
DR ArrayExpress; Q3YEC7; -.
DR Bgee; Q3YEC7; -.
DR Genevestigator; Q3YEC7; -.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR013684; MIRO-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF08477; Miro; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Glycoprotein; GTP-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 729 Rab-like protein 6.
FT /FTId=PRO_0000274223.
FT NP_BIND 50 57 GTP (Potential).
FT NP_BIND 100 104 GTP (Potential).
FT NP_BIND 177 179 GTP (Potential).
FT REGION 39 279 Small GTPase-like.
FT REGION 655 693 Interaction with CDKN2A.
FT COMPBIAS 293 384 Pro-rich.
FT COMPBIAS 645 685 Lys-rich.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 402 402 Phosphoserine.
FT MOD_RES 425 425 Phosphoserine.
FT MOD_RES 427 427 Phosphoserine.
FT MOD_RES 470 470 Phosphoserine (By similarity).
FT MOD_RES 471 471 Phosphoserine (By similarity).
FT MOD_RES 577 577 Phosphoserine.
FT MOD_RES 596 596 Phosphoserine.
FT MOD_RES 599 599 Phosphothreonine.
FT VAR_SEQ 199 199 D -> DS (in isoform 2 and isoform 5).
FT /FTId=VSP_022646.
FT VAR_SEQ 236 302 RETLLRQLETNQLDMDATLEELSVQQETEDQNYGIFLEMME
FT ARSRGHASPLAANGQSPSPGSQSPVV -> KDVRLAQERGC
FT AVVLVSEEVRMPAGWDCCWGRLGWKEGGSQTCPVPALLGRP
FT LLPAEPSPHHWVDYSLESSPLLSCSIP (in isoform
FT 6).
FT /FTId=VSP_042559.
FT VAR_SEQ 236 264 RETLLRQLETNQLDMDATLEELSVQQETE -> VSTHHVGW
FT SGCWSLTSFQVSPV (in isoform 4 and isoform
FT 5).
FT /FTId=VSP_022647.
FT VAR_SEQ 265 729 Missing (in isoform 4 and isoform 5).
FT /FTId=VSP_022648.
FT VAR_SEQ 303 729 Missing (in isoform 6).
FT /FTId=VSP_042560.
FT VAR_SEQ 361 729 LFGTSPATEAAPPPPEPVPAAEGPATVQSVEDFVPDDRLDR
FT SFLEDTTPARDEKKVGAKAAQQDSDSDGEALGGNPMVAGFQ
FT DDVDLEDQPRGSPPLPAGPVPSQDITLSSEEEAEVAAPTKG
FT PAPAPQQCSEPETKWSSIPASKPRRGTAPTRTAAPPWPGGV
FT SVRTGPEKRSSTRPPAEMEPGKGEQASSSESDPEGPIAAQM
FT LSFVMDDPDFESEGSDTQRRADDFPVRDDPSDVTDEDEGPA
FT EPPPPPKLPLPAFRLKNDSDLFGLGLEEAGPKESSEEGKEG
FT KTPSKEKKKKKKKGKEEEEKAAKKKSKHKKSKDKEEGKEER
FT RRRQQRPPRSRERTAADELEAFLGGGAPGGRHPGGGDYEEL
FT -> PPPWGWRLRGALGRRGQWPPWGGGRACHCLGRHLPLYH
FT RLCRCPVAAVCASELEEAGHWWSPGWALQVLGLQAQCEPAL
FT QEGRGQLASARLGGHPGPLGAEPPVFLRDVTEAQEGPVRVC
FT LQRLGRGRLAVGCALPRHLLALRAHLGPQHAYGSASGREP
FT (in isoform 3).
FT /FTId=VSP_022649.
FT VARIANT 382 382 E -> Q (in dbSNP:rs2811741).
FT /FTId=VAR_030210.
FT CONFLICT 137 137 Y -> C (in Ref. 7; BAB14408).
SQ SEQUENCE 729 AA; 79549 MW; 6C3FDB38C7FD7D59 CRC64;
MFSALKKLVG SDQAPGRDKN IPAGLQSMNQ ALQRRFAKGV QYNMKIVIRG DRNTGKTALW
HRLQGRPFVE EYIPTQEIQV TSIHWSYKTT DDIVKVEVWD VVDKGKCKKR GDGLKMENDP
QEAESEMALD AEFLDVYKNC NGVVMMFDIT KQWTFNYILR ELPKVPTHVP VCVLGNYRDM
GEHRVILPDD VRDFIDNLDR PPGSSYFRYA ESSMKNSFGL KYLHKFFNIP FLQLQRETLL
RQLETNQLDM DATLEELSVQ QETEDQNYGI FLEMMEARSR GHASPLAANG QSPSPGSQSP
VVPAGAVSTG SSSPGTPQPA PQLPLNAAPP SSVPPVPPSE ALPPPACPSA PAPRRSIISR
LFGTSPATEA APPPPEPVPA AEGPATVQSV EDFVPDDRLD RSFLEDTTPA RDEKKVGAKA
AQQDSDSDGE ALGGNPMVAG FQDDVDLEDQ PRGSPPLPAG PVPSQDITLS SEEEAEVAAP
TKGPAPAPQQ CSEPETKWSS IPASKPRRGT APTRTAAPPW PGGVSVRTGP EKRSSTRPPA
EMEPGKGEQA SSSESDPEGP IAAQMLSFVM DDPDFESEGS DTQRRADDFP VRDDPSDVTD
EDEGPAEPPP PPKLPLPAFR LKNDSDLFGL GLEEAGPKES SEEGKEGKTP SKEKKKKKKK
GKEEEEKAAK KKSKHKKSKD KEEGKEERRR RQQRPPRSRE RTAADELEAF LGGGAPGGRH
PGGGDYEEL
//
ID RABL6_HUMAN Reviewed; 729 AA.
AC Q3YEC7; A8QVZ7; A8QVZ8; C6K8I4; C6K8I5; Q4F968; Q5T5R7; Q8IWK1;
read moreAC Q8TCL4; Q8WU94; Q96SR8; Q9BU21; Q9H935;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 22-JAN-2014, entry version 92.
DE RecName: Full=Rab-like protein 6;
DE AltName: Full=GTP-binding protein Parf;
DE AltName: Full=Partner of ARF;
DE AltName: Full=Rab-like protein 1;
DE Short=RBEL1;
GN Name=RABL6; Synonyms=C9orf86, PARF;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-382, FUNCTION,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CDKN2A.
RX PubMed=16582619;
RA Tompkins V., Hagen J., Zediak V.P., Quelle D.E.;
RT "Identification of novel ARF binding proteins by two-hybrid
RT screening.";
RL Cell Cycle 5:641-646(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), ALTERNATIVE SPLICING,
RP GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=17962191; DOI=10.1074/jbc.M704760200;
RA Montalbano J., Jin W., Sheikh M.S., Huang Y.;
RT "RBEL1 is a novel gene that encodes a nucleocytoplasmic Ras
RT superfamily GTP-binding protein and is overexpressed in breast
RT cancer.";
RL J. Biol. Chem. 282:37640-37649(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 6), AND SUBCELLULAR
RP LOCATION.
RX PubMed=19433581; DOI=10.1074/jbc.M109.009597;
RA Montalbano J., Lui K., Sheikh M.S., Huang Y.;
RT "Identification and characterization of RBEL1 subfamily of GTPases in
RT the Ras superfamily involved in cell growth regulation.";
RL J. Biol. Chem. 284:18129-18142(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-382.
RA Lin L., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA Wen S., Zhou G., Yang S.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
RP VARIANT GLN-382.
RC TISSUE=Brain, and Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-729 (ISOFORM 5),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-729 (ISOFORM 1), AND
RP VARIANT GLN-382.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 251-719.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-577; SER-596 AND
RP THR-599, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425 AND SER-427, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-427; SER-596
RP AND THR-599, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-427; SER-596
RP AND THR-599, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May enhance cellular proliferation. May reduce growth
CC inhibitory activity of CDKN2A.
CC -!- INTERACTION:
CC Q99750:MDFI; NbExp=2; IntAct=EBI-742029, EBI-724076;
CC P58062:SPINK7; NbExp=3; IntAct=EBI-742029, EBI-1182445;
CC -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Note=Predominantly
CC cytoplasmic.
CC -!- SUBCELLULAR LOCATION: Isoform 3: Nucleus. Note=Predominantly
CC nuclear.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=RBEL1A;
CC IsoId=Q3YEC7-1; Sequence=Displayed;
CC Note=Predominant isoform. Overexpressed in about 67% of primary
CC breast tumors;
CC Name=2;
CC IsoId=Q3YEC7-2; Sequence=VSP_022646;
CC Name=3; Synonyms=RBEL1B;
CC IsoId=Q3YEC7-3; Sequence=VSP_022649;
CC Note=No experimental confirmation available;
CC Name=4; Synonyms=RBEL1D;
CC IsoId=Q3YEC7-4; Sequence=VSP_022647, VSP_022648;
CC Name=5;
CC IsoId=Q3YEC7-5; Sequence=VSP_022646, VSP_022647, VSP_022648;
CC Name=6; Synonyms=RBEL1C;
CC IsoId=Q3YEC7-6; Sequence=VSP_042559, VSP_042560;
CC -!- PTM: Isoform 1 is O-glycosylated, while other isoforms are not.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02945.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH21095.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH35786.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14408.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB55213.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; DQ141240; AAZ73768.1; -; mRNA.
DR EMBL; EF156752; ABO84837.1; -; mRNA.
DR EMBL; EF156753; ABO84838.1; -; mRNA.
DR EMBL; GQ169126; ACS45171.1; -; mRNA.
DR EMBL; GQ169127; ACS45172.1; -; mRNA.
DR EMBL; AL355987; CAI12685.1; -; Genomic_DNA.
DR EMBL; AL355987; CAI12686.1; -; Genomic_DNA.
DR EMBL; DQ099383; AAZ13759.1; -; mRNA.
DR EMBL; BC002945; AAH02945.2; ALT_INIT; mRNA.
DR EMBL; BC021095; AAH21095.2; ALT_INIT; mRNA.
DR EMBL; BC035786; AAH35786.1; ALT_INIT; mRNA.
DR EMBL; AK023107; BAB14408.1; ALT_INIT; mRNA.
DR EMBL; AK027586; BAB55213.1; ALT_INIT; mRNA.
DR EMBL; AL713707; CAD28504.1; -; mRNA.
DR RefSeq; NP_001167459.1; NM_001173988.1.
DR RefSeq; NP_001167460.1; NM_001173989.2.
DR RefSeq; NP_078994.3; NM_024718.4.
DR UniGene; Hs.370555; -.
DR ProteinModelPortal; Q3YEC7; -.
DR SMR; Q3YEC7; 41-239.
DR IntAct; Q3YEC7; 5.
DR PhosphoSite; Q3YEC7; -.
DR DMDM; 125957950; -.
DR PaxDb; Q3YEC7; -.
DR PRIDE; Q3YEC7; -.
DR Ensembl; ENST00000311502; ENSP00000311134; ENSG00000196642.
DR Ensembl; ENST00000357466; ENSP00000350056; ENSG00000196642.
DR Ensembl; ENST00000371663; ENSP00000360727; ENSG00000196642.
DR Ensembl; ENST00000371671; ENSP00000360736; ENSG00000196642.
DR GeneID; 55684; -.
DR KEGG; hsa:55684; -.
DR UCSC; uc004cji.1; human.
DR CTD; 55684; -.
DR GeneCards; GC09P139702; -.
DR HGNC; HGNC:24703; RABL6.
DR HPA; HPA044037; -.
DR MIM; 610615; gene.
DR neXtProt; NX_Q3YEC7; -.
DR PharmGKB; PA134868176; -.
DR eggNOG; NOG138310; -.
DR HOGENOM; HOG000015428; -.
DR HOVERGEN; HBG080325; -.
DR InParanoid; Q3YEC7; -.
DR PhylomeDB; Q3YEC7; -.
DR ChiTaRS; C9orf86; human.
DR GeneWiki; C9orf86; -.
DR GenomeRNAi; 55684; -.
DR NextBio; 60481; -.
DR PRO; PR:Q3YEC7; -.
DR ArrayExpress; Q3YEC7; -.
DR Bgee; Q3YEC7; -.
DR Genevestigator; Q3YEC7; -.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR013684; MIRO-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF08477; Miro; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Glycoprotein; GTP-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 729 Rab-like protein 6.
FT /FTId=PRO_0000274223.
FT NP_BIND 50 57 GTP (Potential).
FT NP_BIND 100 104 GTP (Potential).
FT NP_BIND 177 179 GTP (Potential).
FT REGION 39 279 Small GTPase-like.
FT REGION 655 693 Interaction with CDKN2A.
FT COMPBIAS 293 384 Pro-rich.
FT COMPBIAS 645 685 Lys-rich.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 402 402 Phosphoserine.
FT MOD_RES 425 425 Phosphoserine.
FT MOD_RES 427 427 Phosphoserine.
FT MOD_RES 470 470 Phosphoserine (By similarity).
FT MOD_RES 471 471 Phosphoserine (By similarity).
FT MOD_RES 577 577 Phosphoserine.
FT MOD_RES 596 596 Phosphoserine.
FT MOD_RES 599 599 Phosphothreonine.
FT VAR_SEQ 199 199 D -> DS (in isoform 2 and isoform 5).
FT /FTId=VSP_022646.
FT VAR_SEQ 236 302 RETLLRQLETNQLDMDATLEELSVQQETEDQNYGIFLEMME
FT ARSRGHASPLAANGQSPSPGSQSPVV -> KDVRLAQERGC
FT AVVLVSEEVRMPAGWDCCWGRLGWKEGGSQTCPVPALLGRP
FT LLPAEPSPHHWVDYSLESSPLLSCSIP (in isoform
FT 6).
FT /FTId=VSP_042559.
FT VAR_SEQ 236 264 RETLLRQLETNQLDMDATLEELSVQQETE -> VSTHHVGW
FT SGCWSLTSFQVSPV (in isoform 4 and isoform
FT 5).
FT /FTId=VSP_022647.
FT VAR_SEQ 265 729 Missing (in isoform 4 and isoform 5).
FT /FTId=VSP_022648.
FT VAR_SEQ 303 729 Missing (in isoform 6).
FT /FTId=VSP_042560.
FT VAR_SEQ 361 729 LFGTSPATEAAPPPPEPVPAAEGPATVQSVEDFVPDDRLDR
FT SFLEDTTPARDEKKVGAKAAQQDSDSDGEALGGNPMVAGFQ
FT DDVDLEDQPRGSPPLPAGPVPSQDITLSSEEEAEVAAPTKG
FT PAPAPQQCSEPETKWSSIPASKPRRGTAPTRTAAPPWPGGV
FT SVRTGPEKRSSTRPPAEMEPGKGEQASSSESDPEGPIAAQM
FT LSFVMDDPDFESEGSDTQRRADDFPVRDDPSDVTDEDEGPA
FT EPPPPPKLPLPAFRLKNDSDLFGLGLEEAGPKESSEEGKEG
FT KTPSKEKKKKKKKGKEEEEKAAKKKSKHKKSKDKEEGKEER
FT RRRQQRPPRSRERTAADELEAFLGGGAPGGRHPGGGDYEEL
FT -> PPPWGWRLRGALGRRGQWPPWGGGRACHCLGRHLPLYH
FT RLCRCPVAAVCASELEEAGHWWSPGWALQVLGLQAQCEPAL
FT QEGRGQLASARLGGHPGPLGAEPPVFLRDVTEAQEGPVRVC
FT LQRLGRGRLAVGCALPRHLLALRAHLGPQHAYGSASGREP
FT (in isoform 3).
FT /FTId=VSP_022649.
FT VARIANT 382 382 E -> Q (in dbSNP:rs2811741).
FT /FTId=VAR_030210.
FT CONFLICT 137 137 Y -> C (in Ref. 7; BAB14408).
SQ SEQUENCE 729 AA; 79549 MW; 6C3FDB38C7FD7D59 CRC64;
MFSALKKLVG SDQAPGRDKN IPAGLQSMNQ ALQRRFAKGV QYNMKIVIRG DRNTGKTALW
HRLQGRPFVE EYIPTQEIQV TSIHWSYKTT DDIVKVEVWD VVDKGKCKKR GDGLKMENDP
QEAESEMALD AEFLDVYKNC NGVVMMFDIT KQWTFNYILR ELPKVPTHVP VCVLGNYRDM
GEHRVILPDD VRDFIDNLDR PPGSSYFRYA ESSMKNSFGL KYLHKFFNIP FLQLQRETLL
RQLETNQLDM DATLEELSVQ QETEDQNYGI FLEMMEARSR GHASPLAANG QSPSPGSQSP
VVPAGAVSTG SSSPGTPQPA PQLPLNAAPP SSVPPVPPSE ALPPPACPSA PAPRRSIISR
LFGTSPATEA APPPPEPVPA AEGPATVQSV EDFVPDDRLD RSFLEDTTPA RDEKKVGAKA
AQQDSDSDGE ALGGNPMVAG FQDDVDLEDQ PRGSPPLPAG PVPSQDITLS SEEEAEVAAP
TKGPAPAPQQ CSEPETKWSS IPASKPRRGT APTRTAAPPW PGGVSVRTGP EKRSSTRPPA
EMEPGKGEQA SSSESDPEGP IAAQMLSFVM DDPDFESEGS DTQRRADDFP VRDDPSDVTD
EDEGPAEPPP PPKLPLPAFR LKNDSDLFGL GLEEAGPKES SEEGKEGKTP SKEKKKKKKK
GKEEEEKAAK KKSKHKKSKD KEEGKEERRR RQQRPPRSRE RTAADELEAF LGGGAPGGRH
PGGGDYEEL
//
MIM
610615
*RECORD*
*FIELD* NO
610615
*FIELD* TI
*610615 PARTNER OF ARF
;;PARF;;
CHROMOSOME 9 OPEN READING FRAME 86; C9ORF86
*FIELD* TX
read more
CLONING
Using the p19(Arf) isoform of mouse Cdkn2a (600160) as bait in a yeast
2-hybrid screen of a mouse embryonic fibroblast cDNA library, followed
by RT-PCR of human brain cDNA, Tompkins et al. (2006) cloned mouse and
human PARF. The deduced 729-amino acid human protein has an N-terminal
GTP-binding domain, followed by a RAB (see 179508)-like domain, 2
proline-rich sequences, and a C-terminal nuclear localization signal.
GENE FUNCTION
Using in vitro and in vivo binding assays, including reciprocal
immunoprecipitation assays, Tompkins et al. (2006) confirmed that PARF
bound p19(ARF), but not the p16(INK4A) isoform of CDKN2A. PARF appeared
to shuttle in and out of the nucleus of transfected human cells.
Knockdown of PARF by RNA interference enhanced the rate of cell
proliferation and reduced the growth inhibitory activity of p19(ARF).
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TBRG1
gene to chromosome 11 (TMAP STS-T95820).
*FIELD* RF
1. Tompkins, V.; Hagen, J.; Zediak, V. P.; Quelle, D. E.: Identification
of novel ARF binding proteins by two-hybrid screening. Cell Cycle 5:
641-646, 2006.
*FIELD* CD
Patricia A. Hartz: 11/29/2006
*FIELD* ED
mgross: 11/29/2006
*RECORD*
*FIELD* NO
610615
*FIELD* TI
*610615 PARTNER OF ARF
;;PARF;;
CHROMOSOME 9 OPEN READING FRAME 86; C9ORF86
*FIELD* TX
read more
CLONING
Using the p19(Arf) isoform of mouse Cdkn2a (600160) as bait in a yeast
2-hybrid screen of a mouse embryonic fibroblast cDNA library, followed
by RT-PCR of human brain cDNA, Tompkins et al. (2006) cloned mouse and
human PARF. The deduced 729-amino acid human protein has an N-terminal
GTP-binding domain, followed by a RAB (see 179508)-like domain, 2
proline-rich sequences, and a C-terminal nuclear localization signal.
GENE FUNCTION
Using in vitro and in vivo binding assays, including reciprocal
immunoprecipitation assays, Tompkins et al. (2006) confirmed that PARF
bound p19(ARF), but not the p16(INK4A) isoform of CDKN2A. PARF appeared
to shuttle in and out of the nucleus of transfected human cells.
Knockdown of PARF by RNA interference enhanced the rate of cell
proliferation and reduced the growth inhibitory activity of p19(ARF).
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TBRG1
gene to chromosome 11 (TMAP STS-T95820).
*FIELD* RF
1. Tompkins, V.; Hagen, J.; Zediak, V. P.; Quelle, D. E.: Identification
of novel ARF binding proteins by two-hybrid screening. Cell Cycle 5:
641-646, 2006.
*FIELD* CD
Patricia A. Hartz: 11/29/2006
*FIELD* ED
mgross: 11/29/2006